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Volumn 75, Issue , 2014, Pages 55-69

Characterization of the GPI-anchored lipid transfer proteins in the moss Physcomitrella patens

Author keywords

Circular dichroism; Cuticle; Cutin; Heat stability; Lipids; LTP; Moss

Indexed keywords

BRYOPHYTA; CHLOROPHYTA; EMBRYOPHYTA; PHYSCOMITRELLA PATENS; PICHIA PASTORIS;

EID: 84891139992     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2013.12.001     Document Type: Article
Times cited : (38)

References (92)
  • 1
    • 0031252084 scopus 로고    scopus 로고
    • Role of arabidopsis MYC and MYB homologs in drought- and abscisic acid-regulated gene expression
    • Abe H., Yamaguchi-Shinozaki K., Urao T., Iwasaki T., Hosokawa D., Shinozaki K. Role of arabidopsis MYC and MYB homologs in drought- and abscisic acid-regulated gene expression. Plant Cell 1997, 9:1859-1868.
    • (1997) Plant Cell , vol.9 , pp. 1859-1868
    • Abe, H.1    Yamaguchi-Shinozaki, K.2    Urao, T.3    Iwasaki, T.4    Hosokawa, D.5    Shinozaki, K.6
  • 2
    • 84864489995 scopus 로고    scopus 로고
    • T-REX: a web server for inferring, validating and visualizing phylogenetic trees and networks
    • Alix B., Boubacar D.A., Vladimir M. T-REX: a web server for inferring, validating and visualizing phylogenetic trees and networks. Nucleic Acids Res. 2012, 40:W573-W579.
    • (2012) Nucleic Acids Res. , vol.40
    • Alix, B.1    Boubacar, D.A.2    Vladimir, M.3
  • 3
    • 59049084550 scopus 로고    scopus 로고
    • Physcomitrella patens has lipoxygenases for both eicosanoid and octadecanoid pathways
    • Anterola A., Gobel C., Hornung E., Sellhorn G., Feussner I., Grimes H. Physcomitrella patens has lipoxygenases for both eicosanoid and octadecanoid pathways. Phytochemistry 2009, 70:40-52.
    • (2009) Phytochemistry , vol.70 , pp. 40-52
    • Anterola, A.1    Gobel, C.2    Hornung, E.3    Sellhorn, G.4    Feussner, I.5    Grimes, H.6
  • 5
    • 77952612160 scopus 로고    scopus 로고
    • Structural stability and surface activity of sunflower 2S albumins and nonspecific lipid transfer protein
    • Berecz B., Mills E.N., Tamás L., Láng F., Shewry P.R., Mackie A.R. Structural stability and surface activity of sunflower 2S albumins and nonspecific lipid transfer protein. J.Agric. Food Chem. 2010, 58:6490-6497.
    • (2010) J.Agric. Food Chem. , vol.58 , pp. 6490-6497
    • Berecz, B.1    Mills, E.N.2    Tamás, L.3    Láng, F.4    Shewry, P.R.5    Mackie, A.R.6
  • 6
    • 11144220083 scopus 로고    scopus 로고
    • Analysis of the aliphatic monomer composition of polyesters associated with Arabidopsis epidermis: occurrence of octadeca-cis-6, cis-9-diene-1,18-dioate as the major component
    • Bonaventure G., Beisson F., Ohlrogge J., Pollard M. Analysis of the aliphatic monomer composition of polyesters associated with Arabidopsis epidermis: occurrence of octadeca-cis-6, cis-9-diene-1,18-dioate as the major component. Plant J. 2004, 40:920-930.
    • (2004) Plant J. , vol.40 , pp. 920-930
    • Bonaventure, G.1    Beisson, F.2    Ohlrogge, J.3    Pollard, M.4
  • 7
    • 41549165147 scopus 로고    scopus 로고
    • Genome-wide analysis of the rice and Arabidopsis non-specific lipid transfer protein (nsLtp) gene families and identification of wheat nsLtp genes by EST data mining
    • Boutrot F., Chantret N., Gautier M.F. Genome-wide analysis of the rice and Arabidopsis non-specific lipid transfer protein (nsLtp) gene families and identification of wheat nsLtp genes by EST data mining. BMC Genom. 2008, 9:86.
    • (2008) BMC Genom. , vol.9 , pp. 86
    • Boutrot, F.1    Chantret, N.2    Gautier, M.F.3
  • 8
    • 84888427477 scopus 로고    scopus 로고
    • An ATP binding cassette transporter is required for cuticular wax deposition and desiccation tolerance in the moss Physcomitrella patens
    • Buda G.J., Barnes W.J., Fich E.A., Park S., Yeats T.H., Zhao L., Domozych D.S., Rose J.K. An ATP binding cassette transporter is required for cuticular wax deposition and desiccation tolerance in the moss Physcomitrella patens. Plant Cell 2013, 10.1105/tpc.113.117648.
    • (2013) Plant Cell
    • Buda, G.J.1    Barnes, W.J.2    Fich, E.A.3    Park, S.4    Yeats, T.H.5    Zhao, L.6    Domozych, D.S.7    Rose, J.K.8
  • 9
    • 79957854402 scopus 로고    scopus 로고
    • Ahundred-year-old question: is the moss calyptra covered by a cuticle? A case study of Funaria hygrometrica
    • Budke J.M., Goffinet B., Jones C.S. Ahundred-year-old question: is the moss calyptra covered by a cuticle? A case study of Funaria hygrometrica. Ann. Bot. 2011, 107:1279-1286.
    • (2011) Ann. Bot. , vol.107 , pp. 1279-1286
    • Budke, J.M.1    Goffinet, B.2    Jones, C.S.3
  • 10
    • 84877310118 scopus 로고    scopus 로고
    • Dehydration protection provided by a maternal cuticle improves offspring fitness in the moss Funaria hygrometrica
    • Budke J.M., Goffinet B., Jones C.S. Dehydration protection provided by a maternal cuticle improves offspring fitness in the moss Funaria hygrometrica. Ann. Bot. 2013, 111:781-789.
    • (2013) Ann. Bot. , vol.111 , pp. 781-789
    • Budke, J.M.1    Goffinet, B.2    Jones, C.S.3
  • 12
    • 0034677790 scopus 로고    scopus 로고
    • Elucidation of determinants of protein stability through genome sequence analysis
    • Chakravarty S., Varadarajan R. Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett. 2000, 470:65-69.
    • (2000) FEBS Lett. , vol.470 , pp. 65-69
    • Chakravarty, S.1    Varadarajan, R.2
  • 13
    • 0034955584 scopus 로고    scopus 로고
    • Promoter analysis of the nuclear gene encoding the chloroplast glyceraldehyde-3-phosphate dehydrogenase B subunit of Arabidopsis thaliana
    • Chan C.S., Guo L., Shih M.C. Promoter analysis of the nuclear gene encoding the chloroplast glyceraldehyde-3-phosphate dehydrogenase B subunit of Arabidopsis thaliana. Plant Mol. Biol. 2001, 46:131-141.
    • (2001) Plant Mol. Biol. , vol.46 , pp. 131-141
    • Chan, C.S.1    Guo, L.2    Shih, M.C.3
  • 14
    • 0028119214 scopus 로고
    • Enhanced recovery of transformants of Agrobacterium tumefaciens after freeze-thaw transformation and drug selection
    • 670
    • Chen H., Nelson R.S., Sherwood J.L. Enhanced recovery of transformants of Agrobacterium tumefaciens after freeze-thaw transformation and drug selection. Biotechniques 1994, 16:664-668. 670.
    • (1994) Biotechniques , vol.16 , pp. 664-668
    • Chen, H.1    Nelson, R.S.2    Sherwood, J.L.3
  • 16
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton L.A., Johnson W.C. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 1986, 155:155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson, W.C.2
  • 17
    • 0031751579 scopus 로고    scopus 로고
    • Structural similarities between surface layers of selected charophycean algae and bryophytes and the cuticles of vascular plants
    • Cook M.E., Graham L.E. Structural similarities between surface layers of selected charophycean algae and bryophytes and the cuticles of vascular plants. Int. J. Plant Sci. 1998, 159:780-787.
    • (1998) Int. J. Plant Sci. , vol.159 , pp. 780-787
    • Cook, M.E.1    Graham, L.E.2
  • 18
    • 33749022803 scopus 로고    scopus 로고
    • Analysis of nanoarchaeumequitans genome and proteome composition: indications for hyperthermophilic and parasitic adaptation
    • Das S., Paul S., Bag S.K., Dutta C. Analysis of nanoarchaeumequitans genome and proteome composition: indications for hyperthermophilic and parasitic adaptation. BMC Genom. 2006, 7:186.
    • (2006) BMC Genom. , vol.7 , pp. 186
    • Das, S.1    Paul, S.2    Bag, S.K.3    Dutta, C.4
  • 19
    • 0002770404 scopus 로고    scopus 로고
    • Soluble derivatives of green fluorescent protein (GFP) for use in Arabidopsis thaliana
    • Davis S.J., Vierstra R.D. Soluble derivatives of green fluorescent protein (GFP) for use in Arabidopsis thaliana. Weeds World 1996, 3:43-48.
    • (1996) Weeds World , vol.3 , pp. 43-48
    • Davis, S.J.1    Vierstra, R.D.2
  • 20
    • 66149161763 scopus 로고    scopus 로고
    • Arabidopsis LTPG is a glycosylphosphatidylinositol-anchored lipid transfer protein required for export of lipids to the plant surface
    • Debono A., Yeats T.H., Rose J.K., Bird D., Jetter R., Kunst L., Samuels L. Arabidopsis LTPG is a glycosylphosphatidylinositol-anchored lipid transfer protein required for export of lipids to the plant surface. Plant Cell 2009, 21:1230-1238.
    • (2009) Plant Cell , vol.21 , pp. 1230-1238
    • Debono, A.1    Yeats, T.H.2    Rose, J.K.3    Bird, D.4    Jetter, R.5    Kunst, L.6    Samuels, L.7
  • 21
    • 0035078262 scopus 로고    scopus 로고
    • Disulfide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2
    • Douliez J.P., Pato C., Rabesona H., Mollé D., Marion D. Disulfide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2. Eur. J. Biochem. 2001, 268:1400-1403.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1400-1403
    • Douliez, J.P.1    Pato, C.2    Rabesona, H.3    Mollé, D.4    Marion, D.5
  • 22
    • 7344261272 scopus 로고    scopus 로고
    • Identification of promoter elements in a low-temperature-responsive gene (blt4.9) from barley (Hordeum vulgare L.)
    • Dunn M.A., White A.J., Vural S., Hughes M.A. Identification of promoter elements in a low-temperature-responsive gene (blt4.9) from barley (Hordeum vulgare L.). Plant Mol. Biol. 1998, 38:551-564.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 551-564
    • Dunn, M.A.1    White, A.J.2    Vural, S.3    Hughes, M.A.4
  • 23
    • 0036931281 scopus 로고    scopus 로고
    • Characterization of germination-specific lipid transfer proteins from Euphorbia lagascae
    • Edqvist J., Farbos I. Characterization of germination-specific lipid transfer proteins from Euphorbia lagascae. Planta 2002, 215:41-50.
    • (2002) Planta , vol.215 , pp. 41-50
    • Edqvist, J.1    Farbos, I.2
  • 25
    • 84887987967 scopus 로고    scopus 로고
    • Coexpression patterns indicate that GPI-anchored non-specific lipid transfer proteins are involved in accumulation of cuticular wax, suberin and sporopollenin
    • Edstam M.M., Blomqvist K., Eklöf A., Wennergren U., Edqvist J. Coexpression patterns indicate that GPI-anchored non-specific lipid transfer proteins are involved in accumulation of cuticular wax, suberin and sporopollenin. Plant Mol. Biol. 2013, 83:625-649.
    • (2013) Plant Mol. Biol. , vol.83 , pp. 625-649
    • Edstam, M.M.1    Blomqvist, K.2    Eklöf, A.3    Wennergren, U.4    Edqvist, J.5
  • 26
    • 82255181327 scopus 로고    scopus 로고
    • Evolutionary history of the non-specific lipid transfer proteins
    • Edstam M.M., Viitanen L., Salminen T.A., Edqvist J. Evolutionary history of the non-specific lipid transfer proteins. Mol. Plant 2011, 4:947-964.
    • (2011) Mol. Plant , vol.4 , pp. 947-964
    • Edstam, M.M.1    Viitanen, L.2    Salminen, T.A.3    Edqvist, J.4
  • 27
    • 0037700887 scopus 로고    scopus 로고
    • Localization of non-specific lipid transfer proteins correlate with programmed cell death responses during endosperm degradation in Euphorbia lagascae seedlings
    • Eklund D.M., Edqvist J. Localization of non-specific lipid transfer proteins correlate with programmed cell death responses during endosperm degradation in Euphorbia lagascae seedlings. Plant Physiol. 2003, 132:1249-1259.
    • (2003) Plant Physiol. , vol.132 , pp. 1249-1259
    • Eklund, D.M.1    Edqvist, J.2
  • 29
    • 0036671216 scopus 로고    scopus 로고
    • Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway
    • Fowler S., Thomashow M.F. Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway. Plant Cell 2002, 14:1675-1690.
    • (2002) Plant Cell , vol.14 , pp. 1675-1690
    • Fowler, S.1    Thomashow, M.F.2
  • 33
    • 0027973368 scopus 로고
    • Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers
    • Gincel E., Simorre J.P., Caille A., Marion D., Ptak M., Vovelle F. Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers. Eur. J. Biochem. 1994, 226:413-422.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 413-422
    • Gincel, E.1    Simorre, J.P.2    Caille, A.3    Marion, D.4    Ptak, M.5    Vovelle, F.6
  • 34
    • 0033607199 scopus 로고    scopus 로고
    • Comparison of lipid binding and transfer properties of two lipid transfer proteins from plants
    • Guerbette F., Grosbois M., Jolliot-Croquin A., Kader J.C., Zachowski A. Comparison of lipid binding and transfer properties of two lipid transfer proteins from plants. Biochemistry 1999, 38:14131-14137.
    • (1999) Biochemistry , vol.38 , pp. 14131-14137
    • Guerbette, F.1    Grosbois, M.2    Jolliot-Croquin, A.3    Kader, J.C.4    Zachowski, A.5
  • 35
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S., Dufayard J.F., Lefort V., Anisimova M., Hordijk W., Gascuel O. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 2010, 59:307-321.
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 36
    • 84878501756 scopus 로고    scopus 로고
    • The rice OsDIL gene plays a role in drought tolerance at vegetative and reproductive stages
    • Guo C., Ge X., Ma H. The rice OsDIL gene plays a role in drought tolerance at vegetative and reproductive stages. Plant Mol. Biol. 2013, 82:239-253.
    • (2013) Plant Mol. Biol. , vol.82 , pp. 239-253
    • Guo, C.1    Ge, X.2    Ma, H.3
  • 37
    • 84876013440 scopus 로고    scopus 로고
    • Lipid transfer protein 3 as a target of MYB96 mediates freezing and drought stress in Arabidopsis
    • Guo L., Yang H., Zhang X., Yang S. Lipid transfer protein 3 as a target of MYB96 mediates freezing and drought stress in Arabidopsis. J.Exp. Bot 2013, 64:1755-1767.
    • (2013) J.Exp. Bot , vol.64 , pp. 1755-1767
    • Guo, L.1    Yang, H.2    Zhang, X.3    Yang, S.4
  • 38
    • 0031097728 scopus 로고    scopus 로고
    • Light regulated transcription in higher plants
    • Hiratsuka K., Chua N.H. Light regulated transcription in higher plants. J.Plant Res. 1997, 110:131-139.
    • (1997) J.Plant Res. , vol.110 , pp. 131-139
    • Hiratsuka, K.1    Chua, N.H.2
  • 39
    • 23844519388 scopus 로고    scopus 로고
    • Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding
    • Hoh F., Pons J.L., Gautier M.F., de Lamotte F., Dumas C. Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding. Acta Crystallogr. Sect. D-Biol. Crystallogr. 2005, 61:397-406.
    • (2005) Acta Crystallogr. Sect. D-Biol. Crystallogr. , vol.61 , pp. 397-406
    • Hoh, F.1    Pons, J.L.2    Gautier, M.F.3    de Lamotte, F.4    Dumas, C.5
  • 40
    • 77953380723 scopus 로고    scopus 로고
    • Does the core circadian clock in the moss Physcomitrella patens (Bryophyta) comprise a single loop?
    • Holm K., Kallman T., Gyllenstrand N., Hedman H., Lagercrantz U. Does the core circadian clock in the moss Physcomitrella patens (Bryophyta) comprise a single loop?. BMC Plant Biol. 2010, 10:109.
    • (2010) BMC Plant Biol. , vol.10 , pp. 109
    • Holm, K.1    Kallman, T.2    Gyllenstrand, N.3    Hedman, H.4    Lagercrantz, U.5
  • 41
    • 16544383025 scopus 로고    scopus 로고
    • Arabidopsis RAV1 is down-regulated by brassinosteroid and may act as a negative regulator during plant development
    • Hu Y.X., Wang Y.X., Liu X.F., Li J.Y. Arabidopsis RAV1 is down-regulated by brassinosteroid and may act as a negative regulator during plant development. Cell Res. 2004, 14:8-15.
    • (2004) Cell Res. , vol.14 , pp. 8-15
    • Hu, Y.X.1    Wang, Y.X.2    Liu, X.F.3    Li, J.Y.4
  • 42
    • 0347859216 scopus 로고    scopus 로고
    • Identification of promoter motifs involved in the network of phytochrome A-regulated gene expression by combined analysis of genomic sequence and microarray data
    • Hudson M.E., Quail P.H. Identification of promoter motifs involved in the network of phytochrome A-regulated gene expression by combined analysis of genomic sequence and microarray data. Plant Physiol. 2003, 133:1605-1616.
    • (2003) Plant Physiol. , vol.133 , pp. 1605-1616
    • Hudson, M.E.1    Quail, P.H.2
  • 43
    • 0036547672 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol (GPI)-anchored proteins
    • Ikezawa H. Glycosylphosphatidylinositol (GPI)-anchored proteins. Biol. Pharm. Bull. 2002, 25:409-417.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 409-417
    • Ikezawa, H.1
  • 44
    • 0016426841 scopus 로고
    • Proteins and the intracellular exchange of lipids. I. Stimulation of phospholipid exchange between mitochondria and microsomal fractions by proteins isolated from potato tuber
    • Kader J.C. Proteins and the intracellular exchange of lipids. I. Stimulation of phospholipid exchange between mitochondria and microsomal fractions by proteins isolated from potato tuber. Biochim. Biophys. Acta 1975, 380:31-44.
    • (1975) Biochim. Biophys. Acta , vol.380 , pp. 31-44
    • Kader, J.C.1
  • 46
    • 84865255383 scopus 로고    scopus 로고
    • Characterization of glycosylphosphatidylinositol-anchored lipid transfer protein 2 (LTPG2) and overlapping function between LTPG/LTPG1 and LTPG2 in cuticular wax export or accumulation in Arabidopsis thaliana
    • Kim H., Lee S.B., Kim H.J., Min M.K., Hwang I., Suh M.C. Characterization of glycosylphosphatidylinositol-anchored lipid transfer protein 2 (LTPG2) and overlapping function between LTPG/LTPG1 and LTPG2 in cuticular wax export or accumulation in Arabidopsis thaliana. Plant Cell Physiol. 2012, 53:1391-1403.
    • (2012) Plant Cell Physiol. , vol.53 , pp. 1391-1403
    • Kim, H.1    Lee, S.B.2    Kim, H.J.3    Min, M.K.4    Hwang, I.5    Suh, M.C.6
  • 47
    • 0001084694 scopus 로고    scopus 로고
    • Isolation of a novel class of bZIP transcription factors that interact with ABA-responsive and embryo-specification elements in the Dc3 promoter using a modified yeast one-hybrid system
    • Kim S.Y., Chung H.J., Thomas T.L. Isolation of a novel class of bZIP transcription factors that interact with ABA-responsive and embryo-specification elements in the Dc3 promoter using a modified yeast one-hybrid system. Plant J. 1997, 11:1237-1251.
    • (1997) Plant J. , vol.11 , pp. 1237-1251
    • Kim, S.Y.1    Chung, H.J.2    Thomas, T.L.3
  • 48
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar S., Tsai C.J., Nussinov R. Factors enhancing protein thermostability. Protein Eng. 2000, 13:179-191.
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 49
    • 70350322116 scopus 로고    scopus 로고
    • Endocytosis of glycosylphosphatidylinositol-anchored proteins
    • Lakhan S.E., Sabharanjak S., De A. Endocytosis of glycosylphosphatidylinositol-anchored proteins. J.Biomed. Sci. 2009, 16:93.
    • (2009) J.Biomed. Sci. , vol.16 , pp. 93
    • Lakhan, S.E.1    Sabharanjak, S.2    De, A.3
  • 50
    • 50049131120 scopus 로고    scopus 로고
    • The structure of "defective in induced resistance" protein of Arabidopsis thaliana, DIR1, reveals a new type of lipid transfer protein
    • Lascombe M.B., Bakan B., Buhot N., Marion D., Blein J.P., Larue V., Lamb C., Prange T. The structure of "defective in induced resistance" protein of Arabidopsis thaliana, DIR1, reveals a new type of lipid transfer protein. Prot. Sci. 2008, 17:1522-1530.
    • (2008) Prot. Sci. , vol.17 , pp. 1522-1530
    • Lascombe, M.B.1    Bakan, B.2    Buhot, N.3    Marion, D.4    Blein, J.P.5    Larue, V.6    Lamb, C.7    Prange, T.8
  • 51
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • Le S.Q., Gascuel O. An improved general amino acid replacement matrix. Mol. Biol. Evol. 2008, 25:1307-1320.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2
  • 52
    • 0032548996 scopus 로고    scopus 로고
    • Rice non-specific lipid transfer protein: the 1.6 A crystal structure in the unliganded state reveals a small hydrophobic cavity
    • Lee J.Y., Min K., Cha H., Shin D.H., Hwang K.Y., Suh S.W. Rice non-specific lipid transfer protein: the 1.6 A crystal structure in the unliganded state reveals a small hydrophobic cavity. J.Mol. Biol. 1998, 276:437-448.
    • (1998) J.Mol. Biol. , vol.276 , pp. 437-448
    • Lee, J.Y.1    Min, K.2    Cha, H.3    Shin, D.H.4    Hwang, K.Y.5    Suh, S.W.6
  • 53
    • 66149095028 scopus 로고    scopus 로고
    • Disruption of glycosylphosphatidylinositol-anchored lipid transfer protein gene altered cuticular lipid composition, increased plastoglobules, and enhanced susceptibility to infection by the fungal pathogen Alternaria brassicicola
    • Lee S.B., Go Y.S., Bae H.J., Park J.H., Cho S.H., Cho H.J., Lee D.S., Park O.K., Hwang I., Suh M. Disruption of glycosylphosphatidylinositol-anchored lipid transfer protein gene altered cuticular lipid composition, increased plastoglobules, and enhanced susceptibility to infection by the fungal pathogen Alternaria brassicicola. Plant Physiol. 2009, 150:42-54.
    • (2009) Plant Physiol. , vol.150 , pp. 42-54
    • Lee, S.B.1    Go, Y.S.2    Bae, H.J.3    Park, J.H.4    Cho, S.H.5    Cho, H.J.6    Lee, D.S.7    Park, O.K.8    Hwang, I.9    Suh, M.10
  • 55
    • 0031700043 scopus 로고    scopus 로고
    • Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins
    • Lerche M.H., Poulsen F.M. Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins. Prot. Sci. 1998, 7:2490-2498.
    • (1998) Prot. Sci. , vol.7 , pp. 2490-2498
    • Lerche, M.H.1    Poulsen, F.M.2
  • 56
    • 17144404580 scopus 로고    scopus 로고
    • Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean
    • Lin K.F., Liu Y.N., Hsu S.T., Samuel D., Cheng C.S., Bonvin A.M., Lyu P.C. Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean. Biochemistry 2005, 44:5703-5712.
    • (2005) Biochemistry , vol.44 , pp. 5703-5712
    • Lin, K.F.1    Liu, Y.N.2    Hsu, S.T.3    Samuel, D.4    Cheng, C.S.5    Bonvin, A.M.6    Lyu, P.C.7
  • 57
    • 0035910388 scopus 로고    scopus 로고
    • Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases
    • Lindorff-Larsen K., Winther J.R. Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases. FEBS Lett. 2001, 488:145-148.
    • (2001) FEBS Lett. , vol.488 , pp. 145-148
    • Lindorff-Larsen, K.1    Winther, J.R.2
  • 59
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley A., Whitmore L., Wallace B.A. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002, 18:211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 60
    • 0037179714 scopus 로고    scopus 로고
    • Aputative lipid transfer protein involved in systemic resistance signalling in Arabidopsis
    • Maldonado A.M., Doerner P., Dixon R.A., Lamb C.J., Cameron R.K. Aputative lipid transfer protein involved in systemic resistance signalling in Arabidopsis. Nature 2002, 419:399-403.
    • (2002) Nature , vol.419 , pp. 399-403
    • Maldonado, A.M.1    Doerner, P.2    Dixon, R.A.3    Lamb, C.J.4    Cameron, R.K.5
  • 61
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan P., Johnson W.C. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 1987, 167:76-85.
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson, W.C.2
  • 62
    • 80155183623 scopus 로고    scopus 로고
    • Selective and programmed cleavage of GPI-anchored proteins from the surface membrane by phospholipase C
    • Müller A., Kloppel C., Smith-Valentine M., Van Houten J., Simon M. Selective and programmed cleavage of GPI-anchored proteins from the surface membrane by phospholipase C. Biochim. Biophys. Acta 2012, 1818:117-124.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 117-124
    • Müller, A.1    Kloppel, C.2    Smith-Valentine, M.3    Van Houten, J.4    Simon, M.5
  • 63
    • 84974883652 scopus 로고
    • Ultrastructure and chemistry of epicuticular wax crystals in Polytrichales sporophytes
    • Neinhuis C., Jetter R. Ultrastructure and chemistry of epicuticular wax crystals in Polytrichales sporophytes. J.Bryol. 1995, 18:399-406.
    • (1995) J.Bryol. , vol.18 , pp. 399-406
    • Neinhuis, C.1    Jetter, R.2
  • 64
    • 0034723470 scopus 로고    scopus 로고
    • Tagged mutagenesis and gene-trap in the moss, Physcomitrella patens by shuttle mutagenesis
    • Nishiyama T., Hiwatashi Y., Sakakibara I., Kato M., Hasebe M. Tagged mutagenesis and gene-trap in the moss, Physcomitrella patens by shuttle mutagenesis. DNA Res. 2000, 7:9-17.
    • (2000) DNA Res. , vol.7 , pp. 9-17
    • Nishiyama, T.1    Hiwatashi, Y.2    Sakakibara, I.3    Kato, M.4    Hasebe, M.5
  • 65
    • 3142632218 scopus 로고    scopus 로고
    • Protein thermostability: structure-based difference of amino acid between thermophilic and mesophilic proteins
    • Pack S.P., Yoo Y.J. Protein thermostability: structure-based difference of amino acid between thermophilic and mesophilic proteins. J.Biotechnol. 2004, 111:269-277.
    • (2004) J.Biotechnol. , vol.111 , pp. 269-277
    • Pack, S.P.1    Yoo, Y.J.2
  • 66
    • 0036007719 scopus 로고    scopus 로고
    • Induction of pepper cDNA encoding a lipid transfer protein during the resistance response to tobacco mosaic virus
    • Park C.J., Shin R., Park J.M., Lee G.J., You J.S., Paek K.H. Induction of pepper cDNA encoding a lipid transfer protein during the resistance response to tobacco mosaic virus. Plant Mol. Biol. 2002, 48:243-254.
    • (2002) Plant Mol. Biol. , vol.48 , pp. 243-254
    • Park, C.J.1    Shin, R.2    Park, J.M.3    Lee, G.J.4    You, J.S.5    Paek, K.H.6
  • 67
    • 0037276059 scopus 로고    scopus 로고
    • Expression studies of SCA in lily and confirmation of its role in pollen tube adhesion
    • Park S.Y., Lord E.M. Expression studies of SCA in lily and confirmation of its role in pollen tube adhesion. Plant Mol. Biol. 2003, 51:183-189.
    • (2003) Plant Mol. Biol. , vol.51 , pp. 183-189
    • Park, S.Y.1    Lord, E.M.2
  • 68
    • 43049153245 scopus 로고    scopus 로고
    • Building lipid barriers: biosynthesis of cutin and suberin
    • Pollard M., Beisson F., Li Y., Ohlrogge J.B. Building lipid barriers: biosynthesis of cutin and suberin. Trends Plant Sci. 2008, 13:236-246.
    • (2008) Trends Plant Sci. , vol.13 , pp. 236-246
    • Pollard, M.1    Beisson, F.2    Li, Y.3    Ohlrogge, J.B.4
  • 69
    • 0038191045 scopus 로고    scopus 로고
    • Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein
    • Pons J.L., de Lamotte F., Gautier M.F., Delsuc M.A. Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein. J.Biol. Chem. 2003, 278:14249-14256.
    • (2003) J.Biol. Chem. , vol.278 , pp. 14249-14256
    • Pons, J.L.1    de Lamotte, F.2    Gautier, M.F.3    Delsuc, M.A.4
  • 70
    • 33745726737 scopus 로고    scopus 로고
    • Lessons in stability from thermophilic proteins
    • Razvi A., Scholtz J.M. Lessons in stability from thermophilic proteins. Prot. Sci. 2006, 15:1569-1578.
    • (2006) Prot. Sci. , vol.15 , pp. 1569-1578
    • Razvi, A.1    Scholtz, J.M.2
  • 71
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J.Mol. Biol. 1993, 234:779-815.
    • (1993) J.Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 72
    • 0037144489 scopus 로고    scopus 로고
    • Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa)
    • Samuel D., Liu Y.J., Cheng C.S., Lyu P.C. Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa). J.Biol. Chem. 2002, 277:35267-35273.
    • (2002) J.Biol. Chem. , vol.277 , pp. 35267-35273
    • Samuel, D.1    Liu, Y.J.2    Cheng, C.S.3    Lyu, P.C.4
  • 74
    • 48549087467 scopus 로고    scopus 로고
    • Proteinase inhibitor from ginkgo seeds is a member of the plant nonspecific lipid transfer protein gene family
    • Sawano Y., Hatano K., Miyakawa T., Komagata H., Miyauchi Y., Yamazaki H., Tanokura M. Proteinase inhibitor from ginkgo seeds is a member of the plant nonspecific lipid transfer protein gene family. Plant Physiol. 2008, 146:1909-1919.
    • (2008) Plant Physiol. , vol.146 , pp. 1909-1919
    • Sawano, Y.1    Hatano, K.2    Miyakawa, T.3    Komagata, H.4    Miyauchi, Y.5    Yamazaki, H.6    Tanokura, M.7
  • 75
    • 51249193668 scopus 로고
    • Arachidonic, 5, 11, 14, 17-eicosatetraenoic and related acids in plants-identification of unsaturated fatty acids
    • Schlenk H., Gellerman J.L. Arachidonic, 5, 11, 14, 17-eicosatetraenoic and related acids in plants-identification of unsaturated fatty acids. J.Am. Oil Chem. Soc. 1965, 42:504-511.
    • (1965) J.Am. Oil Chem. Soc. , vol.42 , pp. 504-511
    • Schlenk, H.1    Gellerman, J.L.2
  • 76
    • 0029643949 scopus 로고
    • High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings
    • Shin D.H., Lee J.Y., Hwang K.Y., Kim K.K., Suh S.W. High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure 1995, 3:189-199.
    • (1995) Structure , vol.3 , pp. 189-199
    • Shin, D.H.1    Lee, J.Y.2    Hwang, K.Y.3    Kim, K.K.4    Suh, S.W.5
  • 78
    • 84881047511 scopus 로고    scopus 로고
    • Molecular dynamics simulations of barley and maize lipid transfer proteins show different ligand binding preferences in agreement with experimental data
    • Smith L.J., Roby Y., Allison J.R., van Gunsteren W.F. Molecular dynamics simulations of barley and maize lipid transfer proteins show different ligand binding preferences in agreement with experimental data. Biochemistry 2013, 52:5029-5038.
    • (2013) Biochemistry , vol.52 , pp. 5029-5038
    • Smith, L.J.1    Roby, Y.2    Allison, J.R.3    van Gunsteren, W.F.4
  • 79
    • 34248653184 scopus 로고    scopus 로고
    • Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants
    • Sparkes I.A., Runions J., Kearns A., Hawes C. Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants. Nat. Protoc. 2006, 1:2019-2025.
    • (2006) Nat. Protoc. , vol.1 , pp. 2019-2025
    • Sparkes, I.A.1    Runions, J.2    Kearns, A.3    Hawes, C.4
  • 80
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000, 287:252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 82
    • 0028428501 scopus 로고
    • Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis
    • Thoma S., Hecht U., Kippers A., Botella J., De Vries S., Somerville C. Tissue-specific expression of a gene encoding a cell wall-localized lipid transfer protein from Arabidopsis. Plant Physiol. 1994, 105:35-45.
    • (1994) Plant Physiol. , vol.105 , pp. 35-45
    • Thoma, S.1    Hecht, U.2    Kippers, A.3    Botella, J.4    De Vries, S.5    Somerville, C.6
  • 83
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 84
    • 34247267633 scopus 로고    scopus 로고
    • Isolation and characterization of a tomato non-specific lipid transfer protein involved in polygalacturonase-mediated pectin degradation
    • Tomassen M.M., Barrett D.M., van der Valk H.C., Woltering E.J. Isolation and characterization of a tomato non-specific lipid transfer protein involved in polygalacturonase-mediated pectin degradation. J.Exp. Bot. 2007, 58:1151-1160.
    • (2007) J.Exp. Bot. , vol.58 , pp. 1151-1160
    • Tomassen, M.M.1    Barrett, D.M.2    van der Valk, H.C.3    Woltering, E.J.4
  • 85
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB: an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L., Wallace B.A. DICHROWEB: an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 2004, 32:W668-W673.
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 86
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases
    • Whitmore L., Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008, 89:392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 89
    • 0038492663 scopus 로고    scopus 로고
    • Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability
    • Xu Z., Liu Y., Yang Y., Jiang W., Arnold E., Ding J. Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability. J.Bact. 2003, 185:4038-4049.
    • (2003) J.Bact. , vol.185 , pp. 4038-4049
    • Xu, Z.1    Liu, Y.2    Yang, Y.3    Jiang, W.4    Arnold, E.5    Ding, J.6
  • 92
    • 38149111171 scopus 로고    scopus 로고
    • Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins
    • Zhou X.X., Wang Y.B., Pan Y.J., Li W.F. Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins. Amino Acids 2008, 34:25-33.
    • (2008) Amino Acids , vol.34 , pp. 25-33
    • Zhou, X.X.1    Wang, Y.B.2    Pan, Y.J.3    Li, W.F.4


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